Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q99497

- PARK7_HUMAN

UniProt

Q99497 - PARK7_HUMAN

Protein

Protein DJ-1

Gene

PARK7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells.15 Publications

    Kineticsi

    1. KM=173.4 µM for casein1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei106 – 10611 Publication
    Active sitei126 – 12611 Publication

    GO - Molecular functioni

    1. androgen receptor binding Source: ParkinsonsUK-UCL
    2. cupric ion binding Source: ParkinsonsUK-UCL
    3. cuprous ion binding Source: ParkinsonsUK-UCL
    4. cytokine binding Source: ParkinsonsUK-UCL
    5. enzyme binding Source: ParkinsonsUK-UCL
    6. identical protein binding Source: ParkinsonsUK-UCL
    7. mRNA binding Source: UniProtKB
    8. oxidoreductase activity, acting on peroxide as acceptor Source: ParkinsonsUK-UCL
    9. peptidase activity Source: UniProtKB
    10. peroxidase activity Source: Ensembl
    11. peroxiredoxin activity Source: Ensembl
    12. protein binding Source: UniProtKB
    13. protein homodimerization activity Source: UniProtKB
    14. receptor binding Source: UniProtKB
    15. scaffold protein binding Source: ParkinsonsUK-UCL
    16. small protein activating enzyme binding Source: ParkinsonsUK-UCL
    17. small protein conjugating enzyme binding Source: ParkinsonsUK-UCL
    18. superoxide dismutase copper chaperone activity Source: ParkinsonsUK-UCL
    19. transcription factor binding Source: ParkinsonsUK-UCL
    20. ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

    GO - Biological processi

    1. adult locomotory behavior Source: Ensembl
    2. autophagy Source: UniProtKB-KW
    3. cellular response to hydrogen peroxide Source: UniProtKB
    4. cellular response to oxidative stress Source: ParkinsonsUK-UCL
    5. dopamine uptake involved in synaptic transmission Source: Ensembl
    6. hydrogen peroxide metabolic process Source: ParkinsonsUK-UCL
    7. inflammatory response Source: UniProtKB-KW
    8. membrane depolarization Source: Ensembl
    9. membrane hyperpolarization Source: Ensembl
    10. mitochondrion organization Source: UniProtKB
    11. negative regulation of cell death Source: UniProtKB
    12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
    13. negative regulation of death-inducing signaling complex assembly Source: ParkinsonsUK-UCL
    14. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
    15. negative regulation of gene expression Source: ParkinsonsUK-UCL
    16. negative regulation of hydrogen peroxide-mediated programmed cell death Source: ParkinsonsUK-UCL
    17. negative regulation of neuron apoptotic process Source: BHF-UCL
    18. negative regulation of neuron death Source: ParkinsonsUK-UCL
    19. negative regulation of protein acetylation Source: ParkinsonsUK-UCL
    20. negative regulation of protein binding Source: UniProtKB
    21. negative regulation of protein export from nucleus Source: ParkinsonsUK-UCL
    22. negative regulation of protein K48-linked deubiquitination Source: ParkinsonsUK-UCL
    23. negative regulation of protein kinase activity Source: ParkinsonsUK-UCL
    24. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
    25. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
    26. negative regulation of TRAIL-activated apoptotic signaling pathway Source: ParkinsonsUK-UCL
    27. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
    28. negative regulation of ubiquitin-specific protease activity Source: ParkinsonsUK-UCL
    29. oxidation-reduction process Source: GOC
    30. positive regulation of androgen receptor activity Source: ParkinsonsUK-UCL
    31. positive regulation of interleukin-8 production Source: ParkinsonsUK-UCL
    32. positive regulation of oxidative phosphorylation uncoupler activity Source: Ensembl
    33. positive regulation of protein homodimerization activity Source: ParkinsonsUK-UCL
    34. positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
    35. positive regulation of superoxide dismutase activity Source: ParkinsonsUK-UCL
    36. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
    37. protein stabilization Source: UniProtKB
    38. regulation of androgen receptor signaling pathway Source: UniProtKB
    39. regulation of inflammatory response Source: UniProtKB
    40. regulation of mitochondrial membrane potential Source: ParkinsonsUK-UCL
    41. regulation of neuron apoptotic process Source: UniProtKB
    42. single fertilization Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Hydrolase, Protease

    Keywords - Biological processi

    Autophagy, Fertilization, Inflammatory response, Stress response

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    SignaLinkiQ99497.

    Protein family/group databases

    MEROPSiC56.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein DJ-1 (EC:3.4.-.-)
    Alternative name(s):
    Oncogene DJ1
    Parkinson disease protein 7
    Gene namesi
    Name:PARK7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:16369. PARK7.

    Subcellular locationi

    Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion
    Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Detected in tau inclusions in brains from neurodegenerative disease patients. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. membrane raft Source: UniProtKB-SubCell
    5. mitochondrion Source: UniProtKB
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: UniProtKB-SubCell
    8. PML body Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Parkinson disease 7 (PARK7) [MIM:606324]: A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 1 Publication
    VAR_020492
    Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 2 Publications
    VAR_020493
    Natural varianti104 – 1041A → T in PARK7. 1 Publication
    VAR_020495
    Natural varianti149 – 1491D → A in PARK7. 1 Publication
    Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
    VAR_020496
    Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 1 Publication
    Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
    VAR_020498

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 461C → A: Reduced localization in lipid rafts; when associated with A-106. 4 Publications
    Mutagenesisi46 – 461C → A: Reduces protein stability. No effect on oxidation. 4 Publications
    Mutagenesisi46 – 461C → S: No effect on mitochondrial translocation. 4 Publications
    Mutagenesisi51 – 511V → A: Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. 1 Publication
    Mutagenesisi53 – 531C → A: Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. 4 Publications
    Mutagenesisi53 – 531C → S: No effect on mitochondrial translocation. 4 Publications
    Mutagenesisi106 – 1061C → A: Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduced binding to OTUD7B. 7 Publications
    Mutagenesisi106 – 1061C → A: Reduced localization in lipid rafts; when associated with A-46. 7 Publications
    Mutagenesisi106 – 1061C → D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. 7 Publications
    Mutagenesisi106 – 1061C → S: No effect on mitochondrial translocation. Reduced protease activity. 7 Publications
    Mutagenesisi126 – 1261H → A: Abolishes protease activity. 1 Publication
    Mutagenesisi130 – 1301K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication
    Mutagenesisi166 – 1661L → P: Reduced localization in lipid rafts. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism, Tumor suppressor

    Organism-specific databases

    MIMi168600. phenotype.
    606324. phenotype.
    Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
    2828. Young adult-onset Parkinsonism.
    PharmGKBiPA32946.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 189Removed in mature formPRO_0000405558
    Chaini1 – ?Protein DJ-1PRO_0000157849

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi46 – 461S-palmitoyl cysteine1 Publication
    Lipidationi53 – 531S-palmitoyl cysteine1 Publication
    Modified residuei67 – 671Phosphotyrosine1 Publication
    Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternate1 Publication
    Lipidationi106 – 1061S-palmitoyl cysteine; alternate1 Publication
    Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei148 – 1481N6-acetyllysineBy similarity
    Modified residuei182 – 1821N6-succinyllysineBy similarity

    Post-translational modificationi

    Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.1 Publication
    Cys-106 is easily oxidized to sulfinic acid.1 Publication
    Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

    Proteomic databases

    MaxQBiQ99497.
    PaxDbiQ99497.
    PeptideAtlasiQ99497.
    PRIDEiQ99497.

    2D gel databases

    OGPiQ99497.
    REPRODUCTION-2DPAGEIPI00298547.
    UCD-2DPAGEO14805.
    Q99497.

    PTM databases

    PhosphoSiteiQ99497.

    Miscellaneous databases

    PMAP-CutDBQ99497.

    Expressioni

    Tissue specificityi

    Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain. Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa.4 Publications

    Inductioni

    By hydrogen peroxide and UV irradiation.2 Publications

    Gene expression databases

    ArrayExpressiQ99497.
    BgeeiQ99497.
    CleanExiHS_PARK7.
    GenevestigatoriQ99497.

    Organism-specific databases

    HPAiCAB005870.
    HPA004190.

    Interactioni

    Subunit structurei

    Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102756EBI-1164361,EBI-608057
    DAXXQ9UER73EBI-1164361,EBI-77321
    FADDQ131589EBI-1164361,EBI-494804
    MTA2O947763EBI-1164361,EBI-1783035
    OTUD7BQ6GQQ93EBI-1164361,EBI-527784

    Protein-protein interaction databases

    BioGridi116446. 61 interactions.
    DIPiDIP-35515N.
    IntActiQ99497. 31 interactions.
    MINTiMINT-5003468.
    STRINGi9606.ENSP00000340278.

    Structurei

    Secondary structure

    1
    189
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi16 – 2813
    Beta strandi32 – 376
    Turni38 – 414
    Beta strandi47 – 493
    Beta strandi51 – 533
    Beta strandi55 – 573
    Helixi58 – 625
    Beta strandi68 – 725
    Helixi76 – 849
    Helixi86 – 9712
    Beta strandi101 – 1055
    Turni106 – 1083
    Helixi109 – 1146
    Helixi127 – 1293
    Helixi130 – 1334
    Turni134 – 1363
    Beta strandi139 – 1413
    Beta strandi145 – 1495
    Beta strandi152 – 1554
    Helixi158 – 1603
    Helixi161 – 17313
    Helixi175 – 1828
    Helixi183 – 1853

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J42X-ray2.50A1-189[»]
    1P5FX-ray1.10A1-189[»]
    1PDVX-ray1.80A1-189[»]
    1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
    1PE0X-ray1.70A/B1-189[»]
    1Q2UX-ray1.60A1-189[»]
    1SOAX-ray1.20A1-189[»]
    1UCFX-ray1.95A/B1-189[»]
    2OR3X-ray1.20A/B1-189[»]
    2R1TX-ray1.70A/B2-188[»]
    2R1UX-ray1.50A/B2-188[»]
    2R1VX-ray1.70A/B2-188[»]
    2RK3X-ray1.05A1-189[»]
    2RK4X-ray1.15A1-189[»]
    2RK6X-ray1.15A1-189[»]
    3B36X-ray1.50A1-189[»]
    3B38X-ray1.85A1-189[»]
    3B3AX-ray1.50A1-189[»]
    3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
    3CY6X-ray1.35A1-189[»]
    3CYFX-ray1.60A1-189[»]
    3CZ9X-ray1.15A1-189[»]
    3CZAX-ray1.20A1-189[»]
    3EZGX-ray1.15A1-189[»]
    3F71X-ray1.20A1-189[»]
    3SF8X-ray1.56A/B1-189[»]
    4BTEX-ray1.38A1-189[»]
    4MNTX-ray1.58A1-189[»]
    4MTCX-ray1.47A1-189[»]
    4N0MX-ray1.95A1-189[»]
    4N12X-ray1.48A1-189[»]
    4OQ4X-ray1.49A1-189[»]
    4P2GX-ray1.35A1-189[»]
    4P34X-ray1.55A1-189[»]
    4P35X-ray1.75A1-189[»]
    4P36X-ray1.18A1-189[»]
    ProteinModelPortaliQ99497.
    SMRiQ99497. Positions 3-188.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99497.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase C56 family.Curated

    Phylogenomic databases

    eggNOGiCOG0693.
    HOGENOMiHOG000063194.
    HOVERGENiHBG053511.
    InParanoidiQ99497.
    KOiK05687.
    OMAiGTTFPFA.
    OrthoDBiEOG7CVPZX.
    PhylomeDBiQ99497.
    TreeFamiTF300119.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    InterProiIPR029062. Class_I_gatase-like.
    IPR006287. DJ1.
    IPR002818. ThiJ/PfpI.
    [Graphical view]
    PfamiPF01965. DJ-1_PfpI. 1 hit.
    [Graphical view]
    SUPFAMiSSF52317. SSF52317. 1 hit.
    TIGRFAMsiTIGR01383. not_thiJ. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q99497-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV    50
    VICPDASLED AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG 100
    LIAAICAGPT ALLAHEIGFG SKVTTHPLAK DKMMNGGHYT YSENRVEKDG 150
    LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD 189
    Length:189
    Mass (Da):19,891
    Last modified:July 5, 2004 - v2
    Checksum:i4B21661B3A76BC67
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti119 – 1191F → C in BAB71782. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 1 Publication
    VAR_020492
    Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 2 Publications
    VAR_020493
    Natural varianti98 – 981R → Q.4 Publications
    Corresponds to variant rs71653619 [ dbSNP | Ensembl ].
    VAR_020494
    Natural varianti104 – 1041A → T in PARK7. 1 Publication
    VAR_020495
    Natural varianti149 – 1491D → A in PARK7. 1 Publication
    Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
    VAR_020496
    Natural varianti150 – 1501G → S.1 Publication
    VAR_020497
    Natural varianti163 – 1631E → K.1 Publication
    VAR_034801
    Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 1 Publication
    Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
    VAR_020498
    Natural varianti171 – 1711A → S.1 Publication
    VAR_020499

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D61380 mRNA. Translation: BAA09603.2.
    AF021819 mRNA. Translation: AAC12806.1.
    AB073864 mRNA. Translation: BAB71782.1.
    AK312000 mRNA. Translation: BAG34938.1.
    AL034417 Genomic DNA. Translation: CAB52550.1.
    CH471130 Genomic DNA. Translation: EAW71591.1.
    BC008188 mRNA. Translation: AAH08188.1.
    AB045294 Genomic DNA. No translation available.
    AY648999 Genomic DNA. Translation: AAT68961.1.
    CCDSiCCDS93.1.
    PIRiJC5394.
    RefSeqiNP_001116849.1. NM_001123377.1.
    NP_009193.2. NM_007262.4.
    XP_005263481.1. XM_005263424.1.
    UniGeneiHs.419640.

    Genome annotation databases

    EnsembliENST00000338639; ENSP00000340278; ENSG00000116288.
    ENST00000377488; ENSP00000366708; ENSG00000116288.
    ENST00000377491; ENSP00000366711; ENSG00000116288.
    ENST00000493373; ENSP00000465404; ENSG00000116288.
    ENST00000493678; ENSP00000418770; ENSG00000116288.
    GeneIDi11315.
    KEGGihsa:11315.
    UCSCiuc001aou.4. human.

    Polymorphism databases

    DMDMi56404943.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D61380 mRNA. Translation: BAA09603.2 .
    AF021819 mRNA. Translation: AAC12806.1 .
    AB073864 mRNA. Translation: BAB71782.1 .
    AK312000 mRNA. Translation: BAG34938.1 .
    AL034417 Genomic DNA. Translation: CAB52550.1 .
    CH471130 Genomic DNA. Translation: EAW71591.1 .
    BC008188 mRNA. Translation: AAH08188.1 .
    AB045294 Genomic DNA. No translation available.
    AY648999 Genomic DNA. Translation: AAT68961.1 .
    CCDSi CCDS93.1.
    PIRi JC5394.
    RefSeqi NP_001116849.1. NM_001123377.1.
    NP_009193.2. NM_007262.4.
    XP_005263481.1. XM_005263424.1.
    UniGenei Hs.419640.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J42 X-ray 2.50 A 1-189 [» ]
    1P5F X-ray 1.10 A 1-189 [» ]
    1PDV X-ray 1.80 A 1-189 [» ]
    1PDW X-ray 2.20 A/B/C/D/E/F/G/H 1-189 [» ]
    1PE0 X-ray 1.70 A/B 1-189 [» ]
    1Q2U X-ray 1.60 A 1-189 [» ]
    1SOA X-ray 1.20 A 1-189 [» ]
    1UCF X-ray 1.95 A/B 1-189 [» ]
    2OR3 X-ray 1.20 A/B 1-189 [» ]
    2R1T X-ray 1.70 A/B 2-188 [» ]
    2R1U X-ray 1.50 A/B 2-188 [» ]
    2R1V X-ray 1.70 A/B 2-188 [» ]
    2RK3 X-ray 1.05 A 1-189 [» ]
    2RK4 X-ray 1.15 A 1-189 [» ]
    2RK6 X-ray 1.15 A 1-189 [» ]
    3B36 X-ray 1.50 A 1-189 [» ]
    3B38 X-ray 1.85 A 1-189 [» ]
    3B3A X-ray 1.50 A 1-189 [» ]
    3BWE X-ray 2.40 A/B/C/D/E/F/G 1-189 [» ]
    3CY6 X-ray 1.35 A 1-189 [» ]
    3CYF X-ray 1.60 A 1-189 [» ]
    3CZ9 X-ray 1.15 A 1-189 [» ]
    3CZA X-ray 1.20 A 1-189 [» ]
    3EZG X-ray 1.15 A 1-189 [» ]
    3F71 X-ray 1.20 A 1-189 [» ]
    3SF8 X-ray 1.56 A/B 1-189 [» ]
    4BTE X-ray 1.38 A 1-189 [» ]
    4MNT X-ray 1.58 A 1-189 [» ]
    4MTC X-ray 1.47 A 1-189 [» ]
    4N0M X-ray 1.95 A 1-189 [» ]
    4N12 X-ray 1.48 A 1-189 [» ]
    4OQ4 X-ray 1.49 A 1-189 [» ]
    4P2G X-ray 1.35 A 1-189 [» ]
    4P34 X-ray 1.55 A 1-189 [» ]
    4P35 X-ray 1.75 A 1-189 [» ]
    4P36 X-ray 1.18 A 1-189 [» ]
    ProteinModelPortali Q99497.
    SMRi Q99497. Positions 3-188.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116446. 61 interactions.
    DIPi DIP-35515N.
    IntActi Q99497. 31 interactions.
    MINTi MINT-5003468.
    STRINGi 9606.ENSP00000340278.

    Protein family/group databases

    MEROPSi C56.002.

    PTM databases

    PhosphoSitei Q99497.

    Polymorphism databases

    DMDMi 56404943.

    2D gel databases

    OGPi Q99497.
    REPRODUCTION-2DPAGE IPI00298547.
    UCD-2DPAGE O14805.
    Q99497.

    Proteomic databases

    MaxQBi Q99497.
    PaxDbi Q99497.
    PeptideAtlasi Q99497.
    PRIDEi Q99497.

    Protocols and materials databases

    DNASUi 11315.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338639 ; ENSP00000340278 ; ENSG00000116288 .
    ENST00000377488 ; ENSP00000366708 ; ENSG00000116288 .
    ENST00000377491 ; ENSP00000366711 ; ENSG00000116288 .
    ENST00000493373 ; ENSP00000465404 ; ENSG00000116288 .
    ENST00000493678 ; ENSP00000418770 ; ENSG00000116288 .
    GeneIDi 11315.
    KEGGi hsa:11315.
    UCSCi uc001aou.4. human.

    Organism-specific databases

    CTDi 11315.
    GeneCardsi GC01P008014.
    GeneReviewsi PARK7.
    HGNCi HGNC:16369. PARK7.
    HPAi CAB005870.
    HPA004190.
    MIMi 168600. phenotype.
    602533. gene.
    606324. phenotype.
    neXtProti NX_Q99497.
    Orphaneti 90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
    2828. Young adult-onset Parkinsonism.
    PharmGKBi PA32946.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0693.
    HOGENOMi HOG000063194.
    HOVERGENi HBG053511.
    InParanoidi Q99497.
    KOi K05687.
    OMAi GTTFPFA.
    OrthoDBi EOG7CVPZX.
    PhylomeDBi Q99497.
    TreeFami TF300119.

    Enzyme and pathway databases

    SignaLinki Q99497.

    Miscellaneous databases

    EvolutionaryTracei Q99497.
    GeneWikii PARK7.
    GenomeRNAii 11315.
    NextBioi 42983.
    PMAP-CutDB Q99497.
    PROi Q99497.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99497.
    Bgeei Q99497.
    CleanExi HS_PARK7.
    Genevestigatori Q99497.

    Family and domain databases

    Gene3Di 3.40.50.880. 1 hit.
    InterProi IPR029062. Class_I_gatase-like.
    IPR006287. DJ1.
    IPR002818. ThiJ/PfpI.
    [Graphical view ]
    Pfami PF01965. DJ-1_PfpI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52317. SSF52317. 1 hit.
    TIGRFAMsi TIGR01383. not_thiJ. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras."
      Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
      Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Cervix carcinoma.
    2. "Homo sapiens RNA-binding protein regulatory subunit mRNA."
      Beaudoin R., Hod Y.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    3. "Human DJ-1 cDNA from PC3 cells."
      Ariga H., Niki T.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Thalamus.
    5. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cervix.
    8. "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
      Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
      Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
      Tissue: Kidney.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "DJ-1 gene G150S mutation."
      Zou H.Q., Chan P.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, VARIANT SER-150.
    11. "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
      Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H.
      J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.
    12. "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system."
      Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R.
      J. Biol. Chem. 278:36588-36595(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    13. "A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization."
      Moore D.J., Zhang L., Dawson T.M., Dawson V.L.
      J. Neurochem. 87:1558-1567(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEGRADATION BY THE PROTEASOME, CHARACTERIZATION OF VARIANTS PARK7 ILE-26 AND PRO-166.
    14. "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."
      Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.
      Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EFCAB6, FUNCTION.
    15. "Immunocytochemical localization of DJ-1 in human male reproductive tissue."
      Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.
      Mol. Reprod. Dev. 66:391-397(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    16. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    17. Cited for: TISSUE SPECIFICITY.
    18. "DJ-1 has a role in antioxidative stress to prevent cell death."
      Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
      EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF VAL-51 AND CYS-53.
    19. "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."
      Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.
      PLoS Biol. 2:1-10(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
      Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
      Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
    22. "DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."
      Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H.
      Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-106.
    23. "DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
      Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
      Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. Cited for: FUNCTION.
    25. "Mitochondrial localization of DJ-1 leads to enhanced neuroprotection."
      Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.
      J. Neurosci. Res. 87:123-129(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
    26. "Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."
      Chen J., Li L., Chin L.S.
      Hum. Mol. Genet. 19:2395-2408(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, MUTAGENESIS OF CYS-106 AND HIS-126.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
      McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
      J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, MUTAGENESIS OF CYS-106.
    29. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
      Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
      Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-106 AND LEU-166.
    30. "Crystal structure of DJ-1/RS and implication on familial Parkinson's disease."
      Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.
      FEBS Lett. 549:171-175(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION.
    31. "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease."
      Tao X., Tong L.
      J. Biol. Chem. 278:31372-31379(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, HOMODIMERIZATION.
    32. "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease."
      Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H., Inagaki F.
      J. Biol. Chem. 278:31380-31384(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), HOMODIMERIZATION.
    33. "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
      Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
      J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106, HOMODIMERIZATION.
    34. "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."
      Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, LACK OF PROTEOLYTIC ACTIVITY.
    35. "The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization."
      Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.
      Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.
    36. "The role of pathogenic DJ-1 mutations in Parkinson's disease."
      Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.
      Ann. Neurol. 54:283-286(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PARK7 ILE-26 AND ALA-149, VARIANT GLN-98.
    37. Cited for: VARIANT PARK7 PRO-166, SUBCELLULAR LOCATION.
    38. Cited for: VARIANT GLN-98.
    39. Cited for: VARIANT PARK7 ASP-64, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
    40. "Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1."
      Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T., Beyer K., Haass C., Kahle P.J.
      J. Biol. Chem. 279:6943-6951(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
    41. Cited for: VARIANT PARK7 THR-104, VARIANTS GLN-98 AND SER-171.
    42. Cited for: VARIANT GLN-98.
    43. Cited for: VARIANT LYS-163.
    44. "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6."
      Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., Chin L.S.
      J. Cell Biol. 178:1025-1038(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT PARK7 PRO-166.
    45. "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
      Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
      PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-64.

    Entry informationi

    Entry nameiPARK7_HUMAN
    AccessioniPrimary (citable) accession number: Q99497
    Secondary accession number(s): B2R4Z1
    , O14805, Q6DR95, Q7LFU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 7, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3